Solid-state NMR spectroscopy is one of the most commonly used techniques to study the
atomic-resolution structure and dynamics of various chemical, biological, material, and …

Since the first pioneering studies on small deuterated peptides dating more than 20 years
ago, 1H detection has evolved into the most efficient approach for investigation of …

The field of paramagnetic NMR has expanded considerably in recent years. This review
addresses both the theoretical description of paramagnetic NMR, and the way in which it is …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has
focused on highly deuterated samples, in which only a small number of protons are …

Using a set of six 1H-detected triple-resonance NMR experiments, we establish a method for
sequence-specific backbone resonance assignment of magic angle spinning (MAS) nuclear …

Solid‐state NMR spectroscopy is an emerging tool for structural studies of crystalline,
membrane‐associated, sedimented, and fibrillar proteins. A major limitation for many studies …

Magic-angle spinning solid-state NMR spectroscopy is an important technique to study
molecular structure, dynamics and interactions, and is rapidly gaining importance in …

This article reviews the large increase in applications of high-resolution 1H magic-angle
spinning (MAS) solid-state NMR, in particular two-dimensional heteronuclear and …

With the development of NMR methodology and technology during the past decades, solid-
state NMR (ssNMR) has become a particularly important tool for investigating structure and …